[go: up one dir, main page]

WO2014072235A1 - Hydrolysat de collagène et son utilisation - Google Patents

Hydrolysat de collagène et son utilisation Download PDF

Info

Publication number
WO2014072235A1
WO2014072235A1 PCT/EP2013/072894 EP2013072894W WO2014072235A1 WO 2014072235 A1 WO2014072235 A1 WO 2014072235A1 EP 2013072894 W EP2013072894 W EP 2013072894W WO 2014072235 A1 WO2014072235 A1 WO 2014072235A1
Authority
WO
WIPO (PCT)
Prior art keywords
collagen hydrolyzate
collagen
weight
gelatin
dietary supplement
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Ceased
Application number
PCT/EP2013/072894
Other languages
German (de)
English (en)
Inventor
Steffen Oesser
Monika Giesen-Wiese
Hans-Ulrich Frech
Stephan Hausmanns
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Gelita AG
Original Assignee
Gelita AG
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Family has litigation
First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=49578271&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=WO2014072235(A1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Priority to BR112015009473-2A priority Critical patent/BR112015009473B1/pt
Priority to ES13789518.1T priority patent/ES2587928T3/es
Priority to AU2013343685A priority patent/AU2013343685B2/en
Priority to JP2015540142A priority patent/JP6272891B2/ja
Priority to EP13789518.1A priority patent/EP2916855B1/fr
Application filed by Gelita AG filed Critical Gelita AG
Priority to MX2015005649A priority patent/MX2015005649A/es
Priority to RU2015121573A priority patent/RU2671401C2/ru
Priority to CN201380057628.9A priority patent/CN104768566B/zh
Publication of WO2014072235A1 publication Critical patent/WO2014072235A1/fr
Priority to US14/697,759 priority patent/US10364283B2/en
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/341—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins
    • A23J3/342—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of animal proteins of collagen; of gelatin
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
    • A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17—Amino acids, peptides or proteins
    • A23L33/18—Peptides; Protein hydrolysates
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
    • A61K35/12—Materials from mammals; Compositions comprising non-specified tissues or cells; Compositions comprising non-embryonic stem cells; Genetically modified cells
    • A61K35/32—Bones; Osteocytes; Osteoblasts; Tendons; Tenocytes; Teeth; Odontoblasts; Cartilage; Chondrocytes; Synovial membrane
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • A61K38/012—Hydrolysed proteins; Derivatives thereof from animals
    • A61K38/014—Hydrolysed proteins; Derivatives thereof from animals from connective tissue peptides, e.g. gelatin, collagen
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
    • A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P19/00—Drugs for skeletal disorders
    • A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
    • A61P19/10—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease for osteoporosis
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/02—Nutrients, e.g. vitamins, minerals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
    • A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs

Definitions

  • the present invention relates to a novel collagen hydrolyzate.
  • the invention further relates to the use of this novel collagen hydrolyzate as an active ingredient for maintaining and / or improving the health of bones, in particular for the prevention and / or treatment of osteoporosis.
  • the invention further relates to a dietary supplement comprising the collagen hydrolyzate.
  • the two essential components of the bone matrix are, on the one hand, a skeleton of cross-linked collagen, which in the case of the bone matrix is type I collagen. Its cross-linking is essentially via the amino acids lysine and hydroxylysine.
  • the second component is hydroxyapatite (also called apatite (CaOH)), which is incorporated into the bone matrix (mineralization of the bones).
  • This structure of the bone is roughly comparable to that of reinforced concrete, in which the properties of the steel framework (corresponding to the collagen) and of the concrete (corresponding to the hydroxyapatite) also complement one another to form an extremely load-bearing structure.
  • osteoporosis In contrast to many other tissue types, the bone has a relatively high regenerative capacity, i. E. The extracellular bone matrix is continuously accumulated and degraded again. In the case of a disturbance of this equilibrium, ie an insufficient build-up of new bone matrix, bone loss occurs. This decrease in bone density is termed osteoporosis and can have various causes. Typically, osteoporosis occurs with increasing age (usually from the beginning of the period) fifth decade), especially common in postmenopausal women (postmenopausal osteoporosis).
  • Collagen hydrolysates obtained by enzymatic hydrolysis of animal collagen each comprise a mixture of peptides of different chain lengths or molecular weights.
  • European Patent EP 0 777 491 B1 discloses e.g. Example, the use of a collagen hydrolyzate having an average molecular weight of 1,000 to 40,000 Da, which is produced by enzymatic hydrolysis of skin collagen, for the treatment of postmenopausal osteoporosis.
  • the present invention is based on the object to propose a collagen hydrolyzate, which has a particularly high efficacy in terms of maintaining and / or improving the health of the bones.
  • a collagen hydrolyzate which is prepared by enzymatic hydrolysis of bone gelatin type B, wherein the collagen hydrolyzate is formed from peptides, of which at least 50 wt.% Have a molecular weight of 1,500 to 13,500 Da, and their average molecular weight in Range from 4,000 to 8,000 Da.
  • Investigations carried out by the inventors on the stimulation of the synthesis of matrix proteins by osteoblasts in vitro, which are described in detail below, have surprisingly shown that such a collagen hydrolyzate has a significantly higher stimulating effect compared to various other hydrolysates, in particular the synthesis of type I collagen.
  • a collagen hydrolyzate in which at least 70% by weight of the peptides have a molecular weight of 1,500 to 13,500 Da and / or whose average molecular weight is in the range from 4,500 to 6,000 Da has proved to be particularly advantageous.
  • a collagen hydrolyzate especially from bone gelatin, especially since the use of hydrolysates from collagen or gelatin from animal skin (especially from pigskin, but also from fish skins) is known from the prior art.
  • gelatin as a denatured, soluble form of collagen is a well-suited starting material for enzymatic hydrolysis.
  • the bone gelatin used in the context of the invention as a starting material for the hydrolyzate is a type B gelatin, which is preferably produced by alkaline digestion of collagen from bones of vertebrates, in particular from ossein. Ossein is defatted and demineralized bone. Conveniently, ossein is used from bovine bone.
  • the isoelectric point (IEP) of the bone gelatine used as starting material is preferably below 5.5.
  • type A gelatins prepared by acid digestion of the collagen have an isoelectric point above 7.
  • the peptides preferably have a degree of amidation of the glutamine or glutamic acid residues and of the aspartic or aspartic acid residues of less than 15% overall, in particular less than 10%.
  • the degree of amidation is thus calculated by dividing the molar proportion of glutamine and asparagine residues the molar proportion of glutamine, glutamic acid, asparagine and aspartic acid residues in the peptides.
  • the latter value results from the natural amino acid composition of the collagen and is typically about 1.12 mmol / g.
  • the molar fraction of the glutamine and asparagine residues can be determined by acidic hydrolysis of the amides and determination of the ammonia formed thereby.
  • a low amidation of the peptides can be achieved in particular by the alkaline digestion of the gelatin used (type B).
  • the collagen hydrolyzate according to the invention having a preferred average molecular weight of 4,600 to 6,000 Da has a higher activity than various lower molecular weight hydrolysates.
  • the molecular weight of the peptides contained also correlates with the viscosity of the collagen hydrolyzate. In this regard, it is preferred if a 20% strength by weight aqueous solution of the collagen hydrolyzate has a viscosity of more than 5 mPa ⁇ s at 25 ° C., in particular more than 6 mPa ⁇ s.
  • the collagen hydrolyzate according to the invention preferably has a content of ammonium, sulfate and phosphate of less than 300 ppm, in particular less than 100 ppm. Correspondingly low salt contents can already be maintained during the preparation of the bone gelatine used for the hydrolysis.
  • collagen hydrolyzate For the enzymatic production of collagen hydrolyzate, various proteases, in particular of microbial origin, can be used, their different specificities for certain amino acids directly influencing the molecular structure of the resulting peptides and thus also their effectiveness. It has been found that a collagen hydrolyzate which is particularly effective with regard to the stimulation of the osteoblasts can preferably be produced by hydrolysis of the gelatin with a neutral endoprotease from Bacillus subtilis. According to a preferred embodiment of the invention, the collagen hydrolyzate is produced by the action of the endoprotease at a temperature of 40 to 60 ° C, in particular about 50 ° C, during a period of 20 to 40 min, in particular about 30 min.
  • the present invention relates, in addition to the above-described collagen hydrolyzate as such, in particular also its use as an active ingredient for maintaining and / or improving the health of bones, in particular for the prevention and / or treatment of osteoporosis. Due to the pronounced stimulating effect of the collagen hydrolyzate according to the invention on the synthesis of matrix proteins by the osteoblasts, which has been confirmed by experiments in vitro, oral administration of the collagen hydrolyzate can specifically counteract a disturbance in the balance between bone formation and degradation.
  • An essential aspect of the invention relates to the use of the collagen hydrolyzate as active ingredient for the prevention and / or treatment of postmenopausal osteoporosis.
  • This form of bone loss is estimated to affect about 50% of women over the age of 50, with up to 20% of bone lost in the first five years after menopause.
  • the present invention thus also relates to a method for the prevention and / or treatment of osteoporosis, in particular postmenopausal osteoporosis, the method comprising the oral administration of the collagen hydrolyzate according to the invention to a patient, in particular to a patient over the age of 50 years.
  • the collagen hydrolyzate according to the invention can be suitably formulated as a dietary supplement.
  • the collagen hydrolyzate may, for example, in the form of a powder, granules, a Solution or a suspension, or in the form of tablets, capsules, capsules or sachets, if necessary in combination with suitable additives or excipients.
  • the collagen hydrolyzate may also be added directly to a food.
  • the daily oral intake is preferably in the range of 1 to 15 g of the collagen hydrolyzate, preferably from 2 to 10 g, more preferably from 2 to 7 g, and especially in the range from 2.5 to 5 g.
  • the appropriate amount can conveniently be formulated as a single daily dose.
  • a further preferred embodiment of the invention relates to a dietary supplement which comprises one or more prebiotics in addition to the collagen hydrolyzate according to the invention.
  • the combination of collagen hydrolyzate with one or more prebiotics is based on the consideration that for a particularly effective regeneration of the bone substance not only the biosynthesis of collagen and other matrix proteins, but also the formation and incorporation of hydroxyapatite in sufficient quantity must be made possible.
  • a limiting factor in this case is the supply of the bone matrix with calcium, whereby not the sufficient intake of calcium with the food is the problem (which is usually guaranteed in a balanced diet), but the sufficient absorption of the absorbed calcium in the intestine, in particular is limited due to the formation of poorly soluble calcium salts.
  • Prebiotics are generally non-digestible food ingredients that specifically stimulate the growth and / or activity of certain micro-organisms of the intestinal flora and thereby have a positive impact on health.
  • Co-administration of collagen hydrolyzate and prebiotics can thus stimulate the formation of the two essential components of the bone matrix and thereby achieve a synergistic effect on bone health, particularly with regard to the prevention and / or treatment of osteoporosis.
  • the dietary supplement according to the invention may in principle comprise any desired weight ratio of collagen hydrolyzate and prebiotic or prebiotics. In order to ensure an adequate supply of both components, however, it is preferred if the proportion of collagen hydrolyzate and prebiotic or the prebiotic each about 20 to about 80 wt.%, More preferably about 40 to about 60 wt. %.
  • the dietary supplement may comprise a mixture of the two components in a weight ratio of about 1: 1.
  • the prebiotic or prebiotics which are used in the dietary supplement according to the invention are preferably selected from oligo- and / or polysaccharides. Oligo- and polysaccharides make up the majority of the known prebiotically active substances, the additional advantageous effect resulting from the use of such substances being that the taste of the dietary supplement is markedly improved compared to pure collagen hydrolyzate.
  • collagen hydrolysates which are commonly referred to as tasteless, can be made by appropriate methods, many consumers perceive a taste impairment termed "glutinous.”
  • the negative flavor components of collagen hydrolyzate can be almost completely eliminated by combination with prebiotic oligo- and / or polysaccharides.
  • the prebiotic (s) are preferably selected from inulin, fructans, galacto-oligosaccharides (GOS), fructo-oligosaccharides (FOS), resistant malatoxtrins, polydextrose and mixtures thereof. These include both naturally occurring and synthetically produced saccharides.
  • Inulin is a fructan that contains up to 100 fructose units and a terminal glucose unit.
  • Fructo-oligosaccharides and galacto-oligosaccharides comprise only fructose or galactose units (usually up to 10)
  • polydextrose is a synthetic polysaccharide of glucose, sorbitol and citric acid units.
  • the dietary supplement comprises as further constituent at least one soluble calcium salt. This ensures at the same time a sufficient supply of the user with calcium, regardless of its other eating habits.
  • the at least one soluble calcium salt is selected from calcium citrate, calcium lactate, calcium gluconate, calcium lactate gluconate, calcium lactobionate, and mixtures thereof.
  • the dietary supplement according to the invention can also contain other components as a combined preparation, which have a positive effect on the health of the bones or which are generally useful as a nutritional supplement. It is particularly favorable z. B., when the dietary supplement further comprises one or more vitamins selected from vitamin C, vitamin D, vitamin D 3 , vitamin E, vitamin K and their metabolites.
  • the dietary supplement according to the invention can also be supplemented by various minerals, in particular fluorochemical, potassium and magnesium salts.
  • various minerals in particular fluorochemical, potassium and magnesium salts.
  • the absorption of such minerals via the intestinal wall can also be supported by short-chain fatty acids.
  • a further advantageous supplement is omega-3 fatty acids, which can lead to an increase in the calcitonin content in the bone. In addition, they are said to have an anti-inflammatory effect.
  • soy isoflavones may have a positive effect on bone density and may be used in the dietary supplement of the present invention.
  • the collagen hydrolyzate according to the invention Due to the positive effect of the collagen hydrolyzate according to the invention on bone health, its administration as a dietary supplement may make it possible to avoid or at least reduce the dose of medicaments which are otherwise used for this purpose, in particular for the prevention and / or treatment of postmenopausal osteoporosis.
  • active pharmaceutical ingredients are selective estrogen receptor modulators (SERM), parathyroid hormone and its analog teriparatite, other hormones (in particular estrogens and growth hormones), bisphosphonates and monoclonal antibodies.
  • a further subject matter of the invention is a method for producing the collagen hydrolyzate according to the invention, comprising the steps:
  • aqueous solution of type B bone gelatin having a concentration of 5 to 20% by weight, in particular about 10% by weight; Addition of a neutral endoprotease from Bacillus subtilis in an amount of 1 to 4 wt.%, In particular about 2 wt.%, Based on the amount of gelatin;
  • the endoprotease is allowed to act on the gelatin at a temperature of 40 to 60 ° C, in particular about 50 ° C, and a pH of 5.5 to 6.5, in particular about 6, during a period of 20 to 40 min, especially about 30 minutes; and thermally inactivating the endoprotease.
  • FIG. 1 shows a gel permeation chromatogram with the molecular weight distribution of a collagen hydrolyzate according to the invention and a comparison hydrolyzate;
  • FIG. 2 a diagram relating to the stimulation of the synthesis of type I collagen and osteocalcin by a collagen hydrolyzate according to the invention and a comparison hydrolyzate;
  • FIG. 3 a diagram relating to the stimulation of the synthesis of various matrix proteins and enzymes by a collagen hydrolyzate according to the invention and four different comparative hydrolysates. Production of collagen hydrolysates
  • B-type gelatin gel hereinafter referred to as bone gelatin
  • Type A pork rind gelatin Two different gelatins were used, namely B-type gelatin gel (hereinafter referred to as bone gelatin) and Type A pork rind gelatin. Their essential parameters are shown in Table 1.
  • the molecular weight distribution of the peptides of the various collagen hydrolysates was determined by gel permeation chromatography using the following parameters:
  • Table 2 shows in each case the molecular weight distribution according to predetermined weight fractions, the average molecular weight, the viscosity and the pH (in each case at 20% by weight and 25 ° C.) and the degree of amidation of the various collagen hydrolysates.
  • FIG. 1 shows the gel permeation chromatogram with the molecular weight distribution of the collagen hydrolyzate according to the invention according to the example and of the collagen hydrolyzate according to Comparative Example 4.
  • the molecular weight is plotted on the abscissa with a logarithmic scale.
  • the human osteoblasts were isolated from knee joints by incubating bone material under vigorous agitation at 37 ° C for 1 h in Hanks solution was supplemented with 7 mg / ml hyaluronidase type I and III-S and

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Veterinary Medicine (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Behavior & Ethology (AREA)
  • Public Health (AREA)
  • Zoology (AREA)
  • Epidemiology (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Organic Chemistry (AREA)
  • General Chemical & Material Sciences (AREA)
  • Rheumatology (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Orthopedic Medicine & Surgery (AREA)
  • Physical Education & Sports Medicine (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Immunology (AREA)
  • Biomedical Technology (AREA)
  • Nutrition Science (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Polymers & Plastics (AREA)
  • Food Science & Technology (AREA)
  • Biochemistry (AREA)
  • Molecular Biology (AREA)
  • Biotechnology (AREA)
  • Virology (AREA)
  • Cell Biology (AREA)
  • Developmental Biology & Embryology (AREA)
  • Mycology (AREA)
  • Biophysics (AREA)
  • Toxicology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Genetics & Genomics (AREA)
  • Hematology (AREA)
  • Diabetes (AREA)
  • Obesity (AREA)

Abstract

La présente invention concerne un hydrolysat de collagène obtenu par hydrolyse enzymatique de gélatine d'os de type B. L'hydrolysat de collagène est constitué de peptides dont au moins 50% en poids, en particulier au moins 70% en poids possèdent une masse moléculaire de 1 500 à 3 500 Da et dont la masse moléculaire moyenne se situe dans la plage de 4 000 à 8 000 Da, en particulier dans la plage de 4 500 à 6 000 Da. L'invention concerne en outre l'utilisation de cet hydrolysat de collagène comme substance active pour préserver et/ou améliorer la santé des os, en particulier pour prévenir et/ou traiter l'ostéoporose. L'invention concerne également un complément alimentaire contenant l'hydrolysat de collagène.
PCT/EP2013/072894 2012-11-06 2013-11-04 Hydrolysat de collagène et son utilisation Ceased WO2014072235A1 (fr)

Priority Applications (9)

Application Number Priority Date Filing Date Title
CN201380057628.9A CN104768566B (zh) 2012-11-06 2013-11-04 胶原水解物及其用途
ES13789518.1T ES2587928T3 (es) 2012-11-06 2013-11-04 Hidrolizado de colágeno y su uso
AU2013343685A AU2013343685B2 (en) 2012-11-06 2013-11-04 Collagen hydrolyzate and use thereof
JP2015540142A JP6272891B2 (ja) 2012-11-06 2013-11-04 コラーゲン加水分解物及びその使用
EP13789518.1A EP2916855B1 (fr) 2012-11-06 2013-11-04 Hydrolysat de collagène et son utilisation
BR112015009473-2A BR112015009473B1 (pt) 2012-11-06 2013-11-04 Hidrolisado de colágeno, seu processo para produção e suplemento alimentar
MX2015005649A MX2015005649A (es) 2012-11-06 2013-11-04 Hidrolizado de colageno y uso del mismo.
RU2015121573A RU2671401C2 (ru) 2012-11-06 2013-11-04 Гидролизат коллагена и его применение
US14/697,759 US10364283B2 (en) 2012-11-06 2015-04-28 Collagen hydrolysate and use thereof

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
DE102012110612.6 2012-11-06
DE102012110612.6A DE102012110612A1 (de) 2012-11-06 2012-11-06 Kollagenhydrolysat und dessen Verwendung

Related Child Applications (1)

Application Number Title Priority Date Filing Date
US14/697,759 Continuation US10364283B2 (en) 2012-11-06 2015-04-28 Collagen hydrolysate and use thereof

Publications (1)

Publication Number Publication Date
WO2014072235A1 true WO2014072235A1 (fr) 2014-05-15

Family

ID=49578271

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/EP2013/072894 Ceased WO2014072235A1 (fr) 2012-11-06 2013-11-04 Hydrolysat de collagène et son utilisation

Country Status (13)

Country Link
US (1) US10364283B2 (fr)
EP (1) EP2916855B1 (fr)
JP (1) JP6272891B2 (fr)
CN (1) CN104768566B (fr)
AU (1) AU2013343685B2 (fr)
BR (1) BR112015009473B1 (fr)
CL (1) CL2015001159A1 (fr)
DE (1) DE102012110612A1 (fr)
ES (1) ES2587928T3 (fr)
MX (1) MX2015005649A (fr)
PL (1) PL2916855T3 (fr)
RU (1) RU2671401C2 (fr)
WO (1) WO2014072235A1 (fr)

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2014183989A1 (fr) 2013-05-13 2014-11-20 Gelita Ag Substance active pour le traitement de la sarcopénie
RU2659383C2 (ru) * 2015-10-20 2018-06-29 федеральное государственное автономное образовательное учреждение высшего образования "Казанский (Приволжский) федеральный университет" (ФГАОУ ВО КФУ) Биоактивный гидрогель для регенерации кожи
WO2020127929A1 (fr) 2018-12-21 2020-06-25 Gelita Ag Peptides de collagène de synthèse et obtenus de manière recombinée à efficacité biologique
WO2021083968A1 (fr) 2019-10-31 2021-05-06 Gelita Ag Peptide de collagène optimisé en termes de physiologie alimentaire
US11673940B2 (en) 2018-11-06 2023-06-13 Gelita Ag Recombinant production of a collagen peptide preparation and use thereof

Families Citing this family (18)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE102014117036A1 (de) 2014-11-20 2016-05-25 RenaCare NEPHROMED GmbH Zusammensetzung zur Eiweißsubstitution
DE202014105602U1 (de) 2014-11-20 2015-11-23 RenaCare NEPHROMED GmbH Zusammensetzung zur Eiweißsubstitution
DE102015121923A1 (de) * 2015-12-16 2017-06-22 Gelita Ag Gießmasse und Verfahren für die Herstellung von Gelatineprodukten
GR1009140B (el) * 2016-01-12 2017-10-20 Σωτηρης Γεωργιου Χορτομαρης Συμπληρωμα διατροφης με χοιρινο και βοϊο κολλαγονο υδρολυμενο και ζελατινη
EP3411016B1 (fr) 2016-02-03 2024-09-11 Fresenius Kabi Deutschland GmbH Formule nutritionelle, hypercaloric et hyperprotidique
NL2017219B1 (en) * 2016-07-22 2018-01-30 Rousselot B V Low cross-linking gelatine
CN110691604A (zh) * 2017-03-15 2020-01-14 罗赛洛公司 水解胶原蛋白肽和共生微生物的组合物及其方法
CN107083415A (zh) * 2017-05-27 2017-08-22 四川汇宇生物技术有限公司 一种明胶的生产方法
US11998654B2 (en) 2018-07-12 2024-06-04 Bard Shannon Limited Securing implants and medical devices
DE102018120420A1 (de) * 2018-08-22 2020-02-27 Gelita Ag Proteinriegel
DE102019130196A1 (de) * 2019-11-08 2021-05-12 Gelita Ag Verfahren zur Herstellung von Kollagenpeptiden aus Knochen, und hergestellte Kollagenpeptide
DE102019130197A1 (de) * 2019-11-08 2021-05-12 Gelita Ag Verfahren zur Herstellung von Knochengelatine, und hergestellte Knochengelatine
US20210145764A1 (en) * 2019-11-15 2021-05-20 Brigham Young University Compositions of cannabidiol (cbd), and/or polyphenols, and methods for the prevention and/or treatment of skin, muscle, nerve and inflammatory disorders, and biological factors and functions in mammals
CA3164511A1 (fr) 2020-01-13 2021-07-22 Chathurada GAJADEERA Hydrolysats de collagene de dinde et procedes de preparation
DE102020126594A1 (de) * 2020-10-09 2022-04-14 Gelita Ag Kollagenhydrolysat als Wirkstoff zum Verzögern der Alterung
BE1030791B1 (nl) * 2022-08-31 2024-07-29 Rousselot B V Gebruik van collageenhydrolysaat bij preventie en/of behandeling van post intensive care syndroom (PICS)
DE202023107635U1 (de) 2023-12-22 2024-02-08 RenaCare NEPHROMED GmbH Zusammensetzung zur Eiweißsubstitution
CN120060939B (zh) * 2025-01-26 2025-12-02 大连理工大学 一种纳米孪晶铜电镀添加剂及电镀液

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0777491B1 (fr) 1994-08-23 2004-11-17 Deutsche Gelatine-Fabriken Stoess AG Utilisation de collagene hydrolyse, sans gout, et substance contenant ledit collagene
DE102010060564A1 (de) * 2010-11-15 2012-05-16 Gelita Ag Verwendung von Kollagenhydrolysat zur Verbesserung der Gesundheit der menschlichen Haut, Haare und/oder Nägel
DE102011000997A1 (de) * 2011-03-01 2012-09-06 Gelita Ag Zusammensetzung für Ernährungszwecke

Family Cites Families (19)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1990003788A1 (fr) * 1988-10-14 1990-04-19 Basf Corporation Procede de production d'une poudre comestible sechee par pulverisation, s'ecoulant librement et contenant une huile
US5120761A (en) * 1988-10-14 1992-06-09 Finnan Jeffrey L Method of making a free-flowing spray dried edible powder comprising an oil
JPH09501678A (ja) * 1993-08-13 1997-02-18 ベイヤー、コーポレーション かむ錠剤の芳香増進剤としての加水分解ゼラチン
FR2720067B1 (fr) 1994-05-17 1996-08-02 Dielen Lab Hydrolysat de protéines d'animaux marins, procédé d'obtention et applications.
JP4609807B2 (ja) 1996-03-28 2011-01-12 雪印乳業株式会社 骨強化用医薬、飲食品及び飼料
JPH1112192A (ja) * 1997-06-18 1999-01-19 Zenyaku Kogyo Kk 骨粗鬆症予防・治療剤
US20020025921A1 (en) * 1999-07-26 2002-02-28 Petito George D. Composition and method for growing, protecting, and healing tissues and cells
GB0031065D0 (en) * 2000-12-20 2001-01-31 Univ Cardiff Preservation of cells
GB2418431A (en) * 2004-09-27 2006-03-29 Multigerm Uk Entpr Ltd Metabolically active micro organisms and methods for their production
US7485323B2 (en) * 2005-05-31 2009-02-03 Gelita Ag Process for making a low molecular weight gelatine hydrolysate and gelatine hydrolysate compositions
JP4975751B2 (ja) 2005-10-13 2012-07-11 グ、ジェニファー、エル． ミネラル・コラーゲン・キレートおよびその製造方法と使用方法
JP5689222B2 (ja) * 2006-11-15 2015-03-25 株式会社明治 コラーゲンペプチド組成物及びこれを含有する飲食品
WO2008075333A2 (fr) * 2006-12-18 2008-06-26 Zeev Pam Compositions comestibles utilisées pour prévenir la chute des cheveux
JP2008247809A (ja) 2007-03-30 2008-10-16 Yaizu Suisankagaku Industry Co Ltd コラーゲン錠剤
FR2927336B1 (fr) * 2008-02-12 2010-05-21 Cie Des Peches Saint Malo Sant Hydrolysat de proteines de poissons presentant une activite de stimulation et de maintien du capital osseux, compositions nutraceutiques et pharmacologiques comprenant un tel hydrolysat et procede d'obtention
DE102009030351A1 (de) 2009-06-22 2010-12-23 Gelita Ag Zusammensetzung zur Behandlung von degenerativen Gelenkerkrankungen
CN102094056B (zh) 2009-12-14 2013-04-03 包头东宝生物技术股份有限公司 可溶性胶原蛋白的制备方法
JP5370225B2 (ja) * 2010-03-18 2013-12-18 株式会社デンソーウェーブ ロボットのアーム連結装置
US8603183B2 (en) * 2011-06-22 2013-12-10 Shinn Jyh Ding Bilayered bone graft device

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0777491B1 (fr) 1994-08-23 2004-11-17 Deutsche Gelatine-Fabriken Stoess AG Utilisation de collagene hydrolyse, sans gout, et substance contenant ledit collagene
DE102010060564A1 (de) * 2010-11-15 2012-05-16 Gelita Ag Verwendung von Kollagenhydrolysat zur Verbesserung der Gesundheit der menschlichen Haut, Haare und/oder Nägel
DE102011000997A1 (de) * 2011-03-01 2012-09-06 Gelita Ag Zusammensetzung für Ernährungszwecke

Non-Patent Citations (5)

* Cited by examiner, † Cited by third party
Title
GMEZ-GUILLN M C ET AL: "Functional and bioactive properties of collagen and gelatin from alternative sources: A review", FOOD HYDROCOLLOIDS, ELSEVIER BV, NL, vol. 25, no. 8, 8 February 2011 (2011-02-08), pages 1813 - 1827, XP028255533, ISSN: 0268-005X, [retrieved on 20110215], DOI: 10.1016/J.FOODHYD.2011.02.007 *
OESSER S ET AL: "Stimulation of type II collagen biosynthesis and secretion in bovine chondrocytes cultured with degraded collagen", CELL AND TISSUE RESEARCH, BERLIN, DE, vol. 311, no. 3, 20 March 2003 (2003-03-20), pages 393 - 399, XP002254608 *
S. ABRAM ET AL., AMERICAN JOURNAL OF CLINICAL NUTRITION, vol. 82, 2005, pages 471 - 476
S. OESSER; J. SEIFFERT, CELL TISSUE RESEARCH, 2003, pages 393 - 399
See also references of EP2916855A1

Cited By (7)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2014183989A1 (fr) 2013-05-13 2014-11-20 Gelita Ag Substance active pour le traitement de la sarcopénie
RU2659383C2 (ru) * 2015-10-20 2018-06-29 федеральное государственное автономное образовательное учреждение высшего образования "Казанский (Приволжский) федеральный университет" (ФГАОУ ВО КФУ) Биоактивный гидрогель для регенерации кожи
US11673940B2 (en) 2018-11-06 2023-06-13 Gelita Ag Recombinant production of a collagen peptide preparation and use thereof
WO2020127929A1 (fr) 2018-12-21 2020-06-25 Gelita Ag Peptides de collagène de synthèse et obtenus de manière recombinée à efficacité biologique
DE102019207859A1 (de) 2018-12-21 2020-06-25 Gelita Ag Synthetische und rekombinant hergestellte Kollagenpeptide mit biologischer Wirksamkeit
WO2021083968A1 (fr) 2019-10-31 2021-05-06 Gelita Ag Peptide de collagène optimisé en termes de physiologie alimentaire
US12528857B2 (en) 2019-10-31 2026-01-20 Gelita Ag Nutritionally-optimized collagen peptide

Also Published As

Publication number Publication date
AU2013343685A8 (en) 2015-07-02
RU2671401C2 (ru) 2018-10-31
CN104768566A (zh) 2015-07-08
MX2015005649A (es) 2015-08-20
AU2013343685B2 (en) 2018-03-29
JP2015534812A (ja) 2015-12-07
AU2013343685A1 (en) 2015-05-21
CL2015001159A1 (es) 2015-08-28
EP2916855A1 (fr) 2015-09-16
EP2916855B1 (fr) 2016-07-27
PL2916855T3 (pl) 2017-08-31
DE102012110612A1 (de) 2014-05-08
ES2587928T3 (es) 2016-10-27
US10364283B2 (en) 2019-07-30
US20150232534A1 (en) 2015-08-20
JP6272891B2 (ja) 2018-01-31
BR112015009473A2 (pt) 2017-07-04
BR112015009473B1 (pt) 2022-10-04
CN104768566B (zh) 2018-06-29
RU2015121573A (ru) 2016-12-27

Similar Documents

Publication Publication Date Title
EP2916855B1 (fr) Hydrolysat de collagène et son utilisation
EP2680713B1 (fr) Composition à usage nutritionnel
DE69529873T2 (de) Knochenstärkendes Mittel, Lebensmittel und Getränke enthaltend dieses Mittel
EP0254289B1 (fr) Agent pour le traitement d'arthroses
EP1105002B1 (fr) Melanges d'hydrates de carbone
DE69727332T2 (de) Zubereitungen enthaltend Kollagen, Vitamin D3 und Kalzium zur Verstärkung des Knochens
DE102008036954B4 (de) Verwendung einer Aminozucker enthaltenden Zusammensetzung
EP2785420B1 (fr) Traitement cosmétique de l'hydrolysat de collagène
EP1455803A1 (fr) Composition pharmaceutique pour une utilisation ophtalmologique et rhinologique
EP0874618A1 (fr) Preparation pour stimuler la pousse des cheveux, ameliorer la structure de la peau et/ou regenerer les ongles
DE69935326T2 (de) Zusammensetzungen enthaltend molybden zur steigerung des proteinanabolismus und der entgiftung
EP2996710B1 (fr) Substance active pour le traitement de la sarcopénie
DE69633818T2 (de) Verwendung eines mittels zur zur vorbeugung oder behandlung von durch anomalitäten des knorpelgewebes verursachten erkrankungen
DE60018545T2 (de) Zusammensetzung zur Behandlung von degenerativen Gelenkerkrankungen
DE602004005455T2 (de) Verfahren zur behandlung oder prävention von chronischen wunden und komplette nahrungszusammensetzung mit glycin und/oder leucin zur verwendung darin
DE69522723T2 (de) Antiallergisches Mittel und Nährstoffzusammensetzung, die Glutamin enthalten
JPH11346711A (ja) 健康食品
DE202014007740U1 (de) Arznei- oder Nahrungsergänzungsmittel zur Behandlung und/oder Prophylaxe von Gelenkbeschwerden, Knochenerkrankungen sowie Zellendegeneration und Demenz ( SmartAger® )
DE60200861T2 (de) Verwendungen einer Zusammensetzung enthaltend teilweise hydrolysiertes Fischgelatin
DE19838794A1 (de) Zusammensetzung zur Behandlung von Osteoarthritis und zur nutritiven Behandlung des Gelenkknorpels
DE102012101911A1 (de) Verwendung von Kollagenhydrolysat
EP4248956A2 (fr) Composition pharmaceutique comprenant du cannabidiol
DE202015101782U1 (de) Synergistische Kollagenhydrolysat-Zusammensetzung
EP3445333A1 (fr) Préparation à base de vitamine
DE102011055800A1 (de) Verwendung von Kollagenhydrolysat

Legal Events

Date Code Title Description
121 Ep: the epo has been informed by wipo that ep was designated in this application

Ref document number: 13789518

Country of ref document: EP

Kind code of ref document: A1

REEP Request for entry into the european phase

Ref document number: 2013789518

Country of ref document: EP

WWE Wipo information: entry into national phase

Ref document number: 2013789518

Country of ref document: EP

ENP Entry into the national phase

Ref document number: 2015540142

Country of ref document: JP

Kind code of ref document: A

WWE Wipo information: entry into national phase

Ref document number: MX/A/2015/005649

Country of ref document: MX

WWE Wipo information: entry into national phase

Ref document number: 15102675

Country of ref document: CO

REG Reference to national code

Ref country code: BR

Ref legal event code: B01A

Ref document number: 112015009473

Country of ref document: BR

ENP Entry into the national phase

Ref document number: 2013343685

Country of ref document: AU

Date of ref document: 20131104

Kind code of ref document: A

ENP Entry into the national phase

Ref document number: 2015121573

Country of ref document: RU

Kind code of ref document: A

ENP Entry into the national phase

Ref document number: 112015009473

Country of ref document: BR

Kind code of ref document: A2

Effective date: 20150428